SitesBLAST
Comparing RR42_RS32735 FitnessBrowser__Cup4G11:RR42_RS32735 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
45% identity, 98% coverage: 8:668/674 of query aligns to 2:652/654 of P9WPQ3
- K322 (≠ P326) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Q5LUF3 Propionyl-CoA carboxylase alpha chain; EC 6.4.1.3 from Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) (see paper)
39% identity, 98% coverage: 8:669/674 of query aligns to 2:681/681 of Q5LUF3
- F348 (= F354) binding
- W515 (= W512) mutation to L: No effect on holoenzyme formation.
- L599 (≠ F582) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (= L585) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (≠ D586) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K635) modified: N6-biotinyllysine
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
39% identity, 98% coverage: 8:669/674 of query aligns to 1:646/646 of 3n6rG
- active site: K115 (= K122), K157 (= K164), D180 (≠ E193), H193 (= H214), R219 (= R240), T258 (= T279), E260 (= E281), E273 (= E294), N275 (= N296), R277 (= R298), E281 (= E302), R323 (= R344), G519 (= G549)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M634), K612 (= K635)
7ybuA Human propionyl-coenzyme a carboxylase
37% identity, 99% coverage: 4:669/674 of query aligns to 1:670/670 of 7ybuA
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
49% identity, 65% coverage: 8:444/674 of query aligns to 2:435/442 of 4mv4A
- active site: K116 (= K122), K159 (= K164), D193 (≠ G201), H206 (= H214), R232 (= R240), T271 (= T279), E273 (= E281), E285 (= E294), N287 (= N296), R289 (= R298), E293 (= E302), R335 (= R344)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K164), G164 (= G169), M166 (= M174), E198 (= E206), Y200 (≠ A208), L201 (≠ V209), H233 (= H241), L275 (= L283), E285 (= E294)
- binding magnesium ion: E273 (= E281), E285 (= E294)
P05165 Propionyl-CoA carboxylase alpha chain, mitochondrial; PCCase subunit alpha; Propanoyl-CoA:carbon dioxide ligase subunit alpha; EC 6.4.1.3 from Homo sapiens (Human) (see 6 papers)
37% identity, 99% coverage: 4:669/674 of query aligns to 59:728/728 of P05165
- A75 (= A20) to P: in PA-1; dbSNP:rs794727479
- R77 (= R22) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A83) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (≠ V109) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (= G142) to E: in PA-1
- M229 (= M174) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q242) to R: in PA-1
- D368 (= D313) to G: in PA-1
- M373 (≠ Q318) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G324) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ V343) to R: in PA-1
- R399 (= R344) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P367) to L: in PA-1; dbSNP:rs1443858896
- L532 (= L492) natural variant: Missing (in PA-1)
- V551 (vs. gap) to F: in dbSNP:rs61749895
- W559 (= W512) to L: in PA-1; dbSNP:rs118169528
- G631 (= G577) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (≠ A609) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K635) modified: N6-biotinyllysine; by HLCS
- C712 (≠ A653) natural variant: Missing (in PA-1; loss of biotinylation)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
51% identity, 68% coverage: 8:464/674 of query aligns to 2:456/456 of 8hz4A
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
49% identity, 64% coverage: 11:444/674 of query aligns to 5:436/444 of 2vr1A
- active site: K116 (= K122), K159 (= K164), D194 (≠ G201), H207 (= H214), R233 (= R240), T272 (= T279), E274 (= E281), E286 (= E294), N288 (= N296), R290 (= R298), E294 (= E302), R336 (= R344)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K164), R165 (= R172), M167 (= M174), Y201 (≠ A208), L202 (≠ V209), E274 (= E281), L276 (= L283), E286 (= E294), N288 (= N296), I435 (≠ V443)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
47% identity, 65% coverage: 11:451/674 of query aligns to 3:443/448 of 2vpqB
- active site: V116 (≠ E124), K156 (= K164), H206 (= H214), R232 (= R240), T271 (= T279), E273 (= E281), E287 (= E294), N289 (= N296), R291 (= R298), E295 (= E302), R337 (= R344)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K122), I154 (≠ M162), K156 (= K164), G161 (= G169), G163 (= G171), I166 (≠ M174), F200 (≠ A208), I201 (≠ V209), E273 (= E281), I275 (≠ L283), M286 (= M293), E287 (= E294)
- binding magnesium ion: E273 (= E281), E287 (= E294)
6oi8A Crystal structure of haemophilus influenzae biotin carboxylase complexed with 7-((1r,5s,6s)-6-amino-3-azabicyclo[3.1.0]hexan-3-yl)- 6-(2-chloro-6-(pyridin-3-yl)phenyl)pyrido[2,3-d]pyrimidin-2-amine (see paper)
48% identity, 65% coverage: 8:444/674 of query aligns to 2:433/440 of 6oi8A
- active site: K116 (= K122), K159 (= K164), D191 (≠ G201), H204 (= H214), R230 (= R240), T269 (= T279), E271 (= E281), E283 (= E294), N285 (= N296), R287 (= R298), E291 (= E302), R333 (= R344)
- binding 7-[(1R,5S,6s)-6-amino-3-azabicyclo[3.1.0]hexan-3-yl]-6-[2-chloro-6-(pyridin-3-yl)phenyl]pyrido[2,3-d]pyrimidin-2-amine: I157 (≠ M162), K159 (= K164), M164 (= M174), E196 (= E206), Y198 (≠ A208), L199 (≠ V209), H204 (= H214), Q228 (= Q238), E271 (= E281), L273 (= L283), E283 (= E294), I432 (≠ V443)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
48% identity, 65% coverage: 8:444/674 of query aligns to 2:432/439 of 4mv3A
- active site: K116 (= K122), K159 (= K164), D190 (≠ G201), H203 (= H214), R229 (= R240), T268 (= T279), E270 (= E281), E282 (= E294), N284 (= N296), R286 (= R298), E290 (= E302), R332 (= R344)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K164), M163 (= M174), E195 (= E206), Y197 (≠ A208), L198 (≠ V209), E270 (= E281), L272 (= L283), E282 (= E294)
- binding bicarbonate ion: R286 (= R298), Q288 (= Q300), V289 (= V301)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
48% identity, 66% coverage: 8:452/674 of query aligns to 2:444/447 of 2vqdA
- active site: K116 (= K122), K159 (= K164), P196 (≠ G201), H209 (= H214), R235 (= R240), T274 (= T279), E276 (= E281), E288 (= E294), N290 (= N296), R292 (= R298), E296 (= E302), R338 (= R344)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K122), I157 (≠ M162), K159 (= K164), G164 (= G169), G166 (= G171), F203 (≠ A208), L204 (≠ V209), H209 (= H214), Q233 (= Q238), H236 (= H241), L278 (= L283), E288 (= E294), I437 (≠ T445)
- binding magnesium ion: E276 (= E281), E288 (= E294)
P43873 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see paper)
50% identity, 65% coverage: 8:444/674 of query aligns to 2:438/448 of P43873
- K116 (= K122) binding
- K159 (= K164) binding
- EKYL 201:204 (≠ ERAV 206:209) binding
- E276 (= E281) binding ; binding
- E288 (= E294) binding ; binding
- N290 (= N296) binding
6ojhA Crystal structure of haemophilus influenzae biotin carboxylase complexed with (r)-7-(3-aminopyrrolidin-1-yl)-6-(naphthalen-1-yl) pyrido[2,3-d]pyrimidin-2-amine
50% identity, 64% coverage: 11:444/674 of query aligns to 5:438/445 of 6ojhA
- active site: K116 (= K122), K159 (= K164), D196 (≠ G201), H209 (= H214), R235 (= R240), T274 (= T279), E276 (= E281), E288 (= E294), N290 (= N296), R292 (= R298), E296 (= E302), R338 (= R344)
- binding calcium ion: E276 (= E281), E288 (= E294), N290 (= N296)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K164), M169 (= M174), E201 (= E206), Y203 (≠ A208), L204 (≠ V209), H236 (= H241), L278 (= L283), E288 (= E294), I437 (≠ V443)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
49% identity, 64% coverage: 11:444/674 of query aligns to 5:438/449 of P24182
- R19 (= R25) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (≠ R29) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K122) binding
- K159 (= K164) binding
- GG 165:166 (= GG 170:171) binding
- EKYL 201:204 (≠ ERAV 206:209) binding
- H209 (= H214) binding
- H236 (= H241) binding
- K238 (= K243) binding
- E276 (= E281) binding ; binding
- E288 (= E294) binding ; binding
- R292 (= R298) active site; binding
- V295 (= V301) binding
- E296 (= E302) mutation to A: Severe reduction in catalytic activity.
- R338 (= R344) binding ; binding ; mutation to A: Severe reduction in catalytic activity.
- F363 (≠ H371) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R374) mutation to E: Loss of homodimerization. No effect on ATP binding.
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
49% identity, 64% coverage: 11:444/674 of query aligns to 5:438/444 of 3rupA
- active site: K116 (= K122), K159 (= K164), D196 (≠ G201), H209 (= H214), R235 (= R240), T274 (= T279), E276 (= E281), E288 (= E294), N290 (= N296), R292 (= R298), E296 (= E302), R338 (= R344)
- binding adenosine-5'-diphosphate: Y82 (= Y88), G83 (= G89), K116 (= K122), K159 (= K164), G164 (= G169), G164 (= G169), G165 (= G170), G166 (= G171), R167 (= R172), M169 (= M174), F193 (= F198), E201 (= E206), K202 (≠ R207), Y203 (≠ A208), L204 (≠ V209), H209 (= H214), Q233 (= Q238), H236 (= H241), K238 (= K243), L278 (= L283), E288 (= E294), R292 (= R298), V295 (= V301), E296 (= E302), R338 (= R344), D382 (= D390), I437 (≠ V443)
- binding calcium ion: E87 (= E93), E276 (= E281), E288 (= E294), E288 (= E294), N290 (= N296)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
49% identity, 64% coverage: 11:444/674 of query aligns to 5:438/444 of 3g8cA
- active site: K116 (= K122), K159 (= K164), D196 (≠ G201), H209 (= H214), R235 (= R240), T274 (= T279), E276 (= E281), E288 (= E294), N290 (= N296), R292 (= R298), E296 (= E302), R338 (= R344)
- binding adenosine-5'-diphosphate: I157 (≠ M162), K159 (= K164), G164 (= G169), M169 (= M174), E201 (= E206), K202 (≠ R207), Y203 (≠ A208), L204 (≠ V209), Q233 (= Q238), H236 (= H241), L278 (= L283), E288 (= E294), I437 (≠ V443)
- binding bicarbonate ion: K238 (= K243), R292 (= R298), Q294 (= Q300), V295 (= V301), E296 (= E302)
- binding biotin: Y82 (= Y88), F84 (= F90), R292 (= R298), V295 (= V301), R338 (= R344), D382 (= D390)
- binding magnesium ion: E276 (= E281), E288 (= E294)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
49% identity, 64% coverage: 11:444/674 of query aligns to 5:438/445 of 3jziA
- active site: K116 (= K122), K159 (= K164), D196 (≠ G201), H209 (= H214), R235 (= R240), T274 (= T279), E276 (= E281), E288 (= E294), N290 (= N296), R292 (= R298), E296 (= E302), R338 (= R344)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K122), K159 (= K164), A160 (= A165), G164 (= G169), G165 (= G170), M169 (= M174), Y199 (≠ I204), E201 (= E206), K202 (≠ R207), Y203 (≠ A208), H209 (= H214), Q233 (= Q238), H236 (= H241), L278 (= L283), I287 (≠ M293), E288 (= E294)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
49% identity, 64% coverage: 11:444/674 of query aligns to 5:438/445 of 2w6oA
- active site: K116 (= K122), K159 (= K164), D196 (≠ G201), H209 (= H214), R235 (= R240), T274 (= T279), E276 (= E281), E288 (= E294), N290 (= N296), R292 (= R298), E296 (= E302), R338 (= R344)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K164), K202 (≠ R207), Y203 (≠ A208), L204 (≠ V209), L278 (= L283), I437 (≠ V443)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
49% identity, 64% coverage: 11:444/674 of query aligns to 5:438/445 of 2w6nA
- active site: K116 (= K122), K159 (= K164), D196 (≠ G201), H209 (= H214), R235 (= R240), T274 (= T279), E276 (= E281), E288 (= E294), N290 (= N296), R292 (= R298), E296 (= E302), R338 (= R344)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (≠ M162), K159 (= K164), M169 (= M174), E201 (= E206), K202 (≠ R207), Y203 (≠ A208), L278 (= L283)
Query Sequence
>RR42_RS32735 FitnessBrowser__Cup4G11:RR42_RS32735
MSATSRPFHTLLVANRGEIAMRIMRTARRLGLATVAVYSEADRHGPHVAYADRAVRIGDA
APRASYLNIAAIIEAARRSGADAVHPGYGFLAENAEFADAVAQAGLVFVGPPAAAIRAMG
NKAEAKRLMLAADMPCIPGYQGEAQDDAALLQAAAPIGFPLMVKAAAGGGGRGMRLVHDV
HALPGALASARSEAMAAFGSGQLILERAVIAPRHVEIQVFADTQGHVIHLGERDCSVQRR
HQKVVEEAPSPAVSPALRERMGGAAVRAAQAIGYVGAGTMEFLLDGDGNFYFMEMNTRLQ
VEHAVTEAITGFDLVEWQLRVAAGEPLPVTQEQVALRGHAIEVRLTAEDVAAGFLPQGGP
VLRWRAPGAGHDVRVDHALQEGGEIPVHYDSMVAKLVTHGATREEARRKLLRAVEQTVLL
GVASNQGFLADCLAHEAFAGNQVHTGFVDTHMQAALRTTQPAAAQVACAALAAAGLLAAS
ECPALVAPACSLGLQAGEQQWRVDLRAVAQGWEVAVRGGEGEGEGEGEGDGTSAEIVSVR
VLRADLEQGSALVECNGMALPLVFATGGDAVHLFSAGRAWRFARLDPRQKKRNPGDAGRA
GELLAPLTARIVAVKAAAGEAVLAGQVLVVLEAMKMEHAIVAPFDGVIAQLHAREGGQAR
AGSLLVKVDAGEQA
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory